POPD1_XENTR
ID POPD1_XENTR Reviewed; 338 AA.
AC B1H1G2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Blood vessel epicardial substance;
DE AltName: Full=Popeye domain-containing protein 1;
DE Short=Popeye protein 1;
GN Name=bves; Synonyms=pop1, popdc1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell adhesion molecule involved in the establishment and/or
CC maintenance of cell integrity. May play a role in vamp3-mediated
CC vesicular transport and recycling of different receptor molecules. May
CC be involved in the formation and regulation of the tight junction (TJ)
CC paracellular permeability barrier in epithelial cells. May induce
CC primordial adhesive contact and aggregation of epithelial cells in a
CC Ca(2+)-independent manner. May be involved in epithelial movement
CC during corneal sheet formation and regeneration. May play a role in the
CC regulation of cell shape and movement by modulating the Rho-GTPase
CC activity. May be involved in skeletal muscle and heart development as
CC well as in the maintenance of heart function. May also be involved in
CC striated muscle regeneration and in the regulation of cell spreading
CC (By similarity). {ECO:0000250|UniProtKB:Q5PQZ7,
CC ECO:0000250|UniProtKB:Q8NE79, ECO:0000250|UniProtKB:Q9ES83}.
CC -!- SUBCELLULAR LOCATION: Lateral cell membrane
CC {ECO:0000250|UniProtKB:Q8NE79}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8NE79}. Membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q9ES83}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q9ES83}. Note=Detected at points of cell-cell
CC contact in confluent epithelial sheets. Colocalizes with components of
CC the adherens and tight junctions (By similarity).
CC {ECO:0000250|UniProtKB:Q5PQZ7, ECO:0000250|UniProtKB:Q9ES83}.
CC -!- SIMILARITY: Belongs to the popeye family. {ECO:0000305}.
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DR EMBL; BC160594; AAI60594.1; -; mRNA.
DR RefSeq; NP_001116888.1; NM_001123416.1.
DR AlphaFoldDB; B1H1G2; -.
DR SMR; B1H1G2; -.
DR STRING; 8364.ENSXETP00000029138; -.
DR PaxDb; B1H1G2; -.
DR PRIDE; B1H1G2; -.
DR GeneID; 100144641; -.
DR KEGG; xtr:100144641; -.
DR CTD; 11149; -.
DR Xenbase; XB-GENE-484277; bves.
DR eggNOG; ENOG502QRV2; Eukaryota.
DR HOGENOM; CLU_048494_0_0_1; -.
DR InParanoid; B1H1G2; -.
DR OMA; IDSPEWQ; -.
DR OrthoDB; 1369469at2759; -.
DR TreeFam; TF326644; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; B1H1G2; differential.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; ISS:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
DR GO; GO:0051146; P:striated muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR006916; Popeye_prot.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12101; PTHR12101; 1.
DR Pfam; PF04831; Popeye; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
PE 2: Evidence at transcript level;
KW cAMP; cAMP-binding; Cell adhesion; Cell junction; Cell membrane;
KW Developmental protein; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..338
FT /note="Blood vessel epicardial substance"
FT /id="PRO_0000394482"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 38805 MW; 0EBE70DC8597D105 CRC64;
MATESILITT LPMDLNSQIN NVTFGLNENE TLCENWREIH HLVFHLANTC FAAGLVIPST
LNLHMILLRG MLCLGCIFFI IWAILFRCAL DIMIWNATFL SMNFMHFIYL VYKKRPIKIE
KDLKGIYHRM FEPLHVSPEL FNRLTGQFCE IKTLAKGQTY AIEDKTSVDD RLSILLKGIM
KVSYRGHFLH AISPNAYIDS PEFRSTEMNR GETFQVTITA DDNCVFLCWS RERLTYFLES
EPFLYEIFKY LIGKDITTKL YSLNDPTLGK KKKLDTQPSL CSQLSVMEMR NSLASTSDNE
DGLQTFLRGT STTSSQRNNQ QEFCNAYGVG PLSHAVFC
